Microtubules articles from across Nature Portfolio

Here the authors show that the nucleus undergoes a transient ‘metamorphosis’ within a nuclear–cytoplasmic DNA damage response linked to health and disease. Through this process, the nuclear envelope projects tubules that capture damaged DNA, mediating its repair.

The authors report that the γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation, selectively nucleates microtubules with 13-protofilaments and characterize the structural transformations associated with this function.

The inside surface of microtubules contains so-called microtubule inner proteins, but little is known about their identity. Here the authors use bioinformatics to identify structural motifs within this class of proteins and potential new members.

Centrioles are characterized by an atypical triplet microtubule structure. Here, the authors discover that the ciliopathy protein HYLS1 promotes the assembly of triplet microtubules within human centrioles.

Focal adhesions are dynamic structures that link the cell to the extracellular matrix. Here, the authors report that focal adhesions contain tropomyosin-decorated actin filaments, and show evidence that suggests specific functions in adhesion dynamics and cell migration.

Microtubules are acetylated on the inside of their hollow lumen, a modification linked to their lifespan. Here, the authors show that damage holes act as entry points for a deacetylase to access the lumen, thereby locally counteracting acetylation.

In this Tools of the Trade article, Manuela Richter (Dumont lab) describes a method to probe mechanisms of cytoskeletal network re-organization that uses a targeted laser to both trigger network remodelling and track network dynamics.

Cycles of stretch and compression, such as during cell migration through tissues, lead to stabilization of microtubules owing to redistribution of the plus-end-binding protein CLASP2 along microtubule lengths.

Cell division critically requires amplification of microtubules (MTs) in the bipolar mitotic spindle. This relies on the filamentous augmin complex that enables MT branching. Studies by Gabel et al., Zupa et al. and Travis et al. describe consistent integrated atomic models of the extraordinarily flexible augmin complex. Their work prompts the question: what is this flexibility really needed for?

In this Tools of the Trade article, Patrik Risteski (at Tolić lab) describes high-throughput fluorescent speckle microscopy (FSM) based on a cell-permeable dye that allows to study dynamics of individual microtubules in human cells.

End-binding proteins attach to the dynamic plus-ends of microtubules in order to regulate microtubule polymerization and the transport of other plus-end tracking proteins (+TIPs). Three new studies dissect the multivalent interactions that constitute distinct +TIP networks and reveal that they give rise to liquid-like biomolecular condensates.